Behavior of purified arginine desiminase from S. faecalis

doi:10.1016/0003-9861(57)90485-X

Archives of Biochemistry and Biophysics

Volume 69, 1957, Pages 186-197

https://doi.org/10.1016/0003-9861(57)90485-X Get rights and content

Abstract

Arginine desiminase from S. faecalis has been purified to the extent that 1 mg. catalyzes the hydrolytic cleavage of arginine to citrulline and NH₃ at the rate of 2500 μmoles/hr. (4200 moles/min./100,000 g. at 38 °), proceeding readily to virtual completion. A number of properties of the purified enzyme have been described. Direct evidence of phosphate involvement or of trace-metal ion or pyridoxal phosphate participation in the reaction mechanism has thus far not been obtained.

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Cited by (18)

Immobilization and treatment of Streptococcus faecalis for the continuous conversion of arginine into citrulline
1990, Enzyme and Microbial Technology
Arginine dihydrolase pathway in Lactobacillus buchneri: a review
1988, Biochimie
The arginine dihydrolase system was studied in homo- and hetero-fermentative lactic acid bacteria. This system is widely distributed in Betabacteria lactobacilli subgroup (group II in Bergey's Manual). It is generally absent in the Thermobacterium lactobacilli subgroup (group IA in Bergey's Manual) and also in the Streptobacterium subgroup (group IB in Bergey's Manual). It is present in some species of the genus Streptococcus (groups II, III and IV in Bergey's Manual).
In Lactobacillus buchneri NCDO₁₁₀ the 3 enzymes of the arginine dihydrolase pathway, arginine deiminase, ornithine transcarbamylase and carbamate kinase, were purified and characterized. Arginine deiminase was partially purified (68-fold); ornithine transcarbamylase was also partially purified (14-fold), while carbamate kinase was purified to homogeneity. The apparent molecular weight of the enzymes was 199,000, 162,000 and 97,000 for arginine deiminase, ornithine transcarbamylase and carbamate kinase respectively. For arginine deiminase, maximum enzymatic activity was observed at 50°C and pH 6; for ornithine transcarbamylase it was observed at 35°C and pH 8.5, and for carbamate kinase at 30°C and pH 5.4. The activation energy of the reactions was determined. For arginine deiminase, △G^∗ values were: 8,700 cal mol⁻¹ below 50°C and 380 cal mol⁻¹ above 50°C; for ornithine transcarbamylase, the values were: 9,100 cal mol⁻¹ below 35°C and 4,300 cal mol⁻¹ above 35°C; for carbamate kinase, the activation energy was: 4,078 cal mol⁻¹ for the reaction with Mn²⁺ and 3,059 cal mol⁻¹ for the reaction with Mg²⁺. For characterization of the 3 enzymes, Km values for substrates and Ki values of inhibitors were determined. The results of kinetic analysis of ornithine transcarbamylase are consistent with a ping-pong mechanism. For carbamate kinase, the results of initial velocity studies have indicated that Mn²⁺ ADP was as effective a substrate as Mg²⁺ ADP; and product inhibition studies have shown that the enzyme has 2 distinct sites, one for nucleoside diphosphate and the other for carbamyl phosphate, and that its reaction with the substrates is of the random type.
The formation of the arginine dihydrolase system in Lactobacillus buchneri NCDO₁₁₀ showed that the specific activities of arginine deiminase, ornithine transcarbamylase, and carbamate kinase were higher in galactose-grown cells than in glucose - or sucrose-grown cells. The 3 enzymes were induced by arginine, and this enzymatic system was not repressed by glucose.
Subunit and amino acid composition of L-arginine deiminase of Pseudomonas putida
1978, FEBS Letters
A bio-selective membrane electrode prepared with living bacterial cells
1977, Analytica Chimica Acta
A novel potentiometric sensor has been devised by coupling intact microorganisms (Streptococcus faecium) with an ammonia gas-sensing membrane electrode. The resulting electrode provides a linear response to arginine over the concentration range 5.0 × lO^-5–1. 0 × 10^-3 M in phosphate buffer pH 7.4, with selectivity over other amino acids. The slope of the calibration graph is -40 to -45 mV/decade during the period 2–20 days after preparation. This membrane electrode with living bacterial cells may serve as a model for the development of other new sensing systems.
Regulatory responses of arginine deiminase in whole cells of Clostridium sporogenes
1975, BBA - Enzymology
Arginine deiminase (EC 3.5.3.6) has been shown to have regulatory properties. The activity was observed to be sigmoidal with respect to substrate concentrations. Addition of histidine to the system caused the abolition of sigmoidal responses. The regulatory properties of the enzyme as well as the desensitising action of histidine could also be demonstrated with whole cell suspensions. The pH of the system also seemed to influence modulations in the enzyme.
Determination of argininosuccinate in normal blood serum and liver
1975, Analytical Biochemistry
Argininosuccinate has been determined in normal serum and liver extract of rats by chromatographic analysis on Dowex-1-acetate after a brief period of in vivo labeling with l-[U-¹⁴C] citrulline. The amounts found were within the range of other amino acid intermediates of the ornithine cycle, determined in the same samples. Both ¹⁴C and ninhydrin color were measured. Chromatography on Amberlite columns, subsequent to fractionation on Dowex, allowed determination of the other amino acids. Fractionation on Dowex-1-acetate provides a reliable and highly selective method for the analysis of minute amounts of argininosuccinate in biological samples containing other amino acids.

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^☆: Aided by a Grant from the American Cancer Society.

²: Predoctoral Fellow, The National Heart Institute of the National Institutes of Health.

³: Taken in part from a doctoral dissertation to be submitted to the Faculty of New York University.

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Behavior of purified arginine desiminase from S. faecalis☆

Abstract

Biochem. J

Biochem. J

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J. Biol. Chem

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Arch. Biochem. Biophys

Arch. Biochem. Biophys

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J. Physiol. (London)

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